Journal
PLOS ONE
Volume 5, Issue 12, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0015199
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Funding
- Swedish University of Agricultural Sciences (Sveriges lantbruksuniversitet, SLU)
- NSF
- Agence nationale de la recherche (ANR) [ANR-05-BLAN-0385]
- [SWE-2005-453]
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Background: Fungal mating types in self-incompatible Pezizomycotina are specified by one of two alternate sequences occupying the same locus on corresponding chromosomes. One sequence is characterized by a gene encoding an HMG protein, while the hallmark of the other is a gene encoding a protein with an alpha 1 domain showing similarity to the M protein of Saccharomyces cerevisiae. DNA-binding HMG proteins are ubiquitous and well characterized. In contrast, alpha 1 domain proteins have limited distribution and their evolutionary origin is obscure, precluding a complete understanding of mating-type evolution in Ascomycota. Although much work has focused on the role of the S. cerevisiae Mat alpha 1p protein as a transcription factor, it has not yet been placed in any of the large families of sequence-specific DNA-binding proteins. Methodology/Principal Findings: We present sequence comparisons, phylogenetic analyses, and in silico predictions of secondary and tertiary structures, which support our hypothesis that the alpha 1 domain is related to the HMG domain. We have also characterized a new conserved motif in alpha 1 proteins of Pezizomycotina. This motif is immediately adjacent to and downstream of the alpha 1 domain and consists of a core sequence Y-[LMIF]-x(3)-G-[WL] embedded in a larger conserved motif. Conclusions/Significance: Our data suggest that extant alpha 1-box genes originated from an ancestral HMG gene, which confirms the current model of mating-type evolution within the fungal kingdom. We propose to incorporate alpha 1 proteins in a new subclass of HMG proteins termed MAT alpha_ HMG.
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